Recombinant Δ4,5-Steroid 5β-Reductases as Biocatalysts for the Reduction of Activated C=C-Double Bonds in Monocyclic and Acyclic Molecules

被引：35

作者：

Burda, Edyta ^{[2
]}

Krausser, Marina ^{[2
]}

Fischer, Gabriele ^{[1
]}

Hummel, Werner ^{[3
]}

Mueller-Uri, Frieder ^{[1
]}

Kreis, Wolfgang ^{[1
]}

Groeger, Harald ^{[2
]}

机构：

[1] Univ Erlangen Nurnberg, Dept Biol, D-91058 Erlangen, Germany

[2] Univ Erlangen Nurnberg, Dept Chem & Pharm, D-91054 Erlangen, Germany

[3] Univ Dusseldorf, Res Ctr Julich Stetternicher Forst, Inst Mol Enzyme Technol, D-52426 Julich, Germany

来源：

ADVANCED SYNTHESIS & CATALYSIS | 2009年 / 351卷 / 17期

关键词：

alkenes; biotransformations; enoate reductases; enzyme catalysis; ketones; reduction; OLD YELLOW ENZYME; PENTAERYTHRITOL TETRANITRATE REDUCTASE; ASYMMETRIC BIOREDUCTION; ENOATE REDUCTASES; PROGESTERONE; 5-BETA-REDUCTASE; CANDIDA-MACEDONIENSIS; CRYSTAL-STRUCTURE; NITROALKENES; CLONING;

D O I：

10.1002/adsc.200900024

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

It was found that Delta(4,5)-steroid 5 beta-reductases are capable of reducing also small molecules bearing an activated C=C double bond such as monocyclic enones and acyclic enoate esters. As preferred Delta(4,5)-steroid 5 beta-reductase (5 beta-StR) for this purpose, 5 beta-StR from Arabidopsis thaliana was used. In part. enzyme activities are even higher than that for progesterone. Successful preliminary biotransformations with enzymatic in situ cofactor recycling were also carried out. When using the prochiral compound isophorone as a substrate, a high enantioselective reaction course (>99% ee) was observed.

引用

页码：2787 / 2790

页数：4

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